Life in extreme environments: The role of intrinsically disordered proteins under conditions of abiotic stress
Extremophile organisms have been found in environments once thought unable to sustain life. There has been substantial interest in researching the mechanisms and unlocking the mystery behind these abilities in order to apply new technologies to the preservation of biological materials. Intrinsically disordered proteins (IDPs) are thought to play a key role in stress tolerance because some extremophiles have been found to upregulate these proteins as the organism gains cold and desiccation resistance. Since IDPs are unfolded in their native state, they cannot be denatured by environmental stresses and are hypothesized to interact and stabilize folded cellular proteins under conditions of abiotic stress. Our previous SANS results, at a limited Q range, did not align with the conventional models in literature. The aim of this proposal is to use the D33 SANS instrument with an enhanced Q-range to provide unambiguous data in order to assess a hypothesis of interactions between IDPs and their client proteins in conditions of freeze-stress.
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ROUTH Alexander; GRILLO Isabelle; HOUGH Andrea; TUNNACLIFFE Alan; WATSON Matthew and YUEN Fanny. (2014). Life in extreme environments: The role of intrinsically disordered proteins under conditions of abiotic stress. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-563
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